Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain

The structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by nuclear magnetic resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new...

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Autores principales:	Arán, Martín, Smal, Clara, Gallo, Mariana, Klinke, Sebastián, Mac Cormack, Walter, Turjanski, Adrián Gustavo, Cicero, Daniel Oscar
Publicado:	2014
Materias:	Antarctic bacteria BA42 Bizionia argentinensis Nuclear magnetic resonance Protein structure Structural genomics X-ray crystallography ba42 protein bacterial protein metal ion unclassified drug calcium metal Article beta sheet binding affinity binding site crystal structure Flavobacterium metal binding molecular dynamics nonhuman nuclear magnetic resonance priority journal protein domain protein family protein stability X ray crystallography amino acid sequence animal Antarctica chemical structure chemistry circular dichroism Flavobacteriaceae genetics metabolism molecular genetics protein conformation protein tertiary structure sequence homology Bacteria (microorganisms) Bizionia Amino Acid Sequence Animals Antarctic Regions Bacterial Proteins Binding Sites Calcium Circular Dichroism Crystallography, X-Ray Metals Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Stability Protein Structure, Tertiary Sequence Homology, Amino Acid
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08873585_v82_n11_p3062_Aran http://hdl.handle.net/20.500.12110/paper_08873585_v82_n11_p3062_Aran
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	paper:paper_08873585_v82_n11_p3062_Aran2023-06-08T15:46:48Z Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain Arán, Martín Smal, Clara Gallo, Mariana Klinke, Sebastián Mac Cormack, Walter Turjanski, Adrián Gustavo Cicero, Daniel Oscar Antarctic bacteria BA42 Bizionia argentinensis Nuclear magnetic resonance Protein structure Structural genomics X-ray crystallography ba42 protein bacterial protein metal ion unclassified drug bacterial protein calcium metal Article beta sheet binding affinity binding site Bizionia argentinensis crystal structure Flavobacterium metal binding molecular dynamics nonhuman nuclear magnetic resonance priority journal protein domain protein family protein stability X ray crystallography amino acid sequence animal Antarctica chemical structure chemistry circular dichroism Flavobacteriaceae genetics metabolism molecular genetics protein conformation protein tertiary structure sequence homology Bacteria (microorganisms) Bizionia Flavobacterium Amino Acid Sequence Animals Antarctic Regions Bacterial Proteins Binding Sites Calcium Circular Dichroism Crystallography, X-Ray Flavobacteriaceae Metals Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Stability Protein Structure, Tertiary Sequence Homology, Amino Acid The structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by nuclear magnetic resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new topological variant of the four β-strands constituting the central β-sheet of the αβα architecture and a double metal binding site stabilizing a pair of crossing loops, not observed in previous structures of proteins belonging to this family. BA42 shows differences in structure and dynamics in the presence or absence of bound metals. The affinity for divalent metal ions is close to that observed in proteins that modulate their activity as a function of metal concentration, anticipating a possible role for BA42. © 2014 Wiley Periodicals, Inc. Fil:Aran, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Smal, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gallo, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Klinke, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Mac Cormack, W.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Turjanski, A.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cicero, D.O. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08873585_v82_n11_p3062_Aran http://hdl.handle.net/20.500.12110/paper_08873585_v82_n11_p3062_Aran
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Antarctic bacteria BA42 Bizionia argentinensis Nuclear magnetic resonance Protein structure Structural genomics X-ray crystallography ba42 protein bacterial protein metal ion unclassified drug bacterial protein calcium metal Article beta sheet binding affinity binding site Bizionia argentinensis crystal structure Flavobacterium metal binding molecular dynamics nonhuman nuclear magnetic resonance priority journal protein domain protein family protein stability X ray crystallography amino acid sequence animal Antarctica chemical structure chemistry circular dichroism Flavobacteriaceae genetics metabolism molecular genetics protein conformation protein tertiary structure sequence homology Bacteria (microorganisms) Bizionia Flavobacterium Amino Acid Sequence Animals Antarctic Regions Bacterial Proteins Binding Sites Calcium Circular Dichroism Crystallography, X-Ray Flavobacteriaceae Metals Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Stability Protein Structure, Tertiary Sequence Homology, Amino Acid
spellingShingle	Antarctic bacteria BA42 Bizionia argentinensis Nuclear magnetic resonance Protein structure Structural genomics X-ray crystallography ba42 protein bacterial protein metal ion unclassified drug bacterial protein calcium metal Article beta sheet binding affinity binding site Bizionia argentinensis crystal structure Flavobacterium metal binding molecular dynamics nonhuman nuclear magnetic resonance priority journal protein domain protein family protein stability X ray crystallography amino acid sequence animal Antarctica chemical structure chemistry circular dichroism Flavobacteriaceae genetics metabolism molecular genetics protein conformation protein tertiary structure sequence homology Bacteria (microorganisms) Bizionia Flavobacterium Amino Acid Sequence Animals Antarctic Regions Bacterial Proteins Binding Sites Calcium Circular Dichroism Crystallography, X-Ray Flavobacteriaceae Metals Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Stability Protein Structure, Tertiary Sequence Homology, Amino Acid Arán, Martín Smal, Clara Gallo, Mariana Klinke, Sebastián Mac Cormack, Walter Turjanski, Adrián Gustavo Cicero, Daniel Oscar Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain
topic_facet	Antarctic bacteria BA42 Bizionia argentinensis Nuclear magnetic resonance Protein structure Structural genomics X-ray crystallography ba42 protein bacterial protein metal ion unclassified drug bacterial protein calcium metal Article beta sheet binding affinity binding site Bizionia argentinensis crystal structure Flavobacterium metal binding molecular dynamics nonhuman nuclear magnetic resonance priority journal protein domain protein family protein stability X ray crystallography amino acid sequence animal Antarctica chemical structure chemistry circular dichroism Flavobacteriaceae genetics metabolism molecular genetics protein conformation protein tertiary structure sequence homology Bacteria (microorganisms) Bizionia Flavobacterium Amino Acid Sequence Animals Antarctic Regions Bacterial Proteins Binding Sites Calcium Circular Dichroism Crystallography, X-Ray Flavobacteriaceae Metals Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Stability Protein Structure, Tertiary Sequence Homology, Amino Acid
description	The structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by nuclear magnetic resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new topological variant of the four β-strands constituting the central β-sheet of the αβα architecture and a double metal binding site stabilizing a pair of crossing loops, not observed in previous structures of proteins belonging to this family. BA42 shows differences in structure and dynamics in the presence or absence of bound metals. The affinity for divalent metal ions is close to that observed in proteins that modulate their activity as a function of metal concentration, anticipating a possible role for BA42. © 2014 Wiley Periodicals, Inc.
author	Arán, Martín Smal, Clara Gallo, Mariana Klinke, Sebastián Mac Cormack, Walter Turjanski, Adrián Gustavo Cicero, Daniel Oscar
author_facet	Arán, Martín Smal, Clara Gallo, Mariana Klinke, Sebastián Mac Cormack, Walter Turjanski, Adrián Gustavo Cicero, Daniel Oscar
author_sort	Arán, Martín
title	Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain
title_short	Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain
title_full	Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain
title_fullStr	Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain
title_full_unstemmed	Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain
title_sort	solution and crystal structure of ba42, a protein from the antarctic bacterium bizionia argentinensis comprised of a stand-alone tpm domain
publishDate	2014
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08873585_v82_n11_p3062_Aran http://hdl.handle.net/20.500.12110/paper_08873585_v82_n11_p3062_Aran
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Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain

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